Activation of in situ tissue transglutaminase by intracellular reactive oxygen species

被引：61

作者：

Lee, ZW

Kwon, SM

Kim, SW

Yi, SJ

Kim, YM

Ha, KS ^{[1
]}

机构：

[1] Kangweon Natl Univ, Sch Med, Dept Mol & Cellular Biochem, Chunchon 200701, Kangwon Do, South Korea

[2] Korea Basic Sci Inst, Cell Res Team, Taejon 305333, South Korea

[3] Natl Livestock Res Inst, Div Anim Biotechnol, Suwon 441706, South Korea

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2003年 / 305卷 / 03期

关键词：

reactive oxygen species; tissue transglutaminase; lysophosphatidic acid; transforming growth factor-beta; maitotoxin;

D O I：

10.1016/S0006-291X(03)00835-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We have investigated the novel function of intracellular reactive oxygen species (ROS) in the activation of in situ tissue transglutaminase (tTGase) by lysophosphatidic acid (LPA) and transforming growth factor-beta (TGF-beta) in Swiss 3T3 fibroblasts. LPA induced a transient increase of intracellular ROS with a maximal increase at 10 min, which was blocked by ROS scavengers, N-acetyl-L-cysteine and catalase. LPA activated tTGase with a maximal increase at I It, which was inhibited by cystamine and ROS scavengers. Incubation with exogenous H2O2 activated tTGase. TGF-beta also activated tTGase with a maximal activation at 2 h and the tTGase activation was inhibited by the ROS scavengers. Scrape-loading of C3 transferase inhibited the ROS production and in situ tTGase activation by LPA and TGF-beta, and the inhibitory effect of C3 transferase was reversed by exogenous H2O2. Microinjection of GTPgammaS inhibited transamidating activity of tTGase stimulated by LPA, TGF-beta, and maitotoxin. These results suggested that intracellular ROS was essential for the activation of in situ tTGase in response to LPA and TGF-beta. (C) 2003 Elsevier Science (USA). All rights reserved.

引用

页码：633 / 640

页数：8

共 30 条

[1] Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin [J].